MrNV-pGEX-6P-1

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	Escherichia coli transformed with MrNV-pGEX6P-1 was cultured in Luria-Bertani (LB) broth to the exponential phase. Expression of recombinant protein was induced with 1 mM isopropyl-β-D-thiogalacto-pyranoside for 4 h.

Protocol tips
Escherichia coli transformed with MrNV-pGEX6P-1 was cultured in Luria-Bertani (LB) broth to the exponential phase. Expression of recombinant protein was induced with 1 mM isopropyl-β-D-thiogalacto-pyranoside for 4 h.

Publication protocol

"Escherichia coli transformed with MrNV-pGEX6P-1 was cultured in Luria-Bertani (LB) broth to the
exponential phase. Expression of recombinant protein was induced with 1 mM isopropyl-β-D-thiogalacto-pyranoside for 4 h. After centrifugation at 3000 × g for 20 min at room temperature, the bacterial pellet was resuspended in a buffer containing 100 mM NaH2PO4, 10 mM Tris-HCl, 8 M urea (pH 8)
and 1 mM phenylmethylsulfonyl fluoride and sonicated until a clear lysate was obtained. The lysate was separated using 12% sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). After treatment with 0.3 M KCl, the band of recombinant fusion protein called glutathione-S-transferase (GST)-MrNV was excised and collected in dialysis bags. The recombinant protein was eluted with a Transblot apparatus (BioRad) at 70 V for 6 h and dialyzed in PBS. The protein concentration was determined using the Bradford assay (Bradford 1976). The recombinant protein solutions were adjusted to 0.4 mg ml−1, divided into 0.5 ml aliquots and stored at –70°C."

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